Monoclonal Antibodies Reactive with Different Sites of N and H Antigenic Particles of Poliovirus

Taniguchi, Koki; Urasawa, Shozo; Urasawa, Tomoko

doi:10.1099/0022-1317-64-12-2803

Cited by 8 publications

(8 citation statements)

References 13 publications

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“…Negative staining was carried out in a routine manner as described previously [Taniguchi et al, 1983]. A drop of a virus preparation was placed on a 400-mesh carbon-collodioncoated grid, excess fluid being withdrawn with the edge of a filter paper disk.…”

Section: Electron Microscopymentioning

confidence: 99%

Isolation and characterisation of poliovirus mutants resistant to heating at 50°c for 30 min

Shiomi

Urasawa

et al. 2004

Journal of Medical Virology

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Poliovirus is heat-labile; on heating at 50 degrees Celsius for 30 min its infectivity decreases drastically and its antigenicity reverts from N to H. However, mutants resistant to heating at 50 degrees Celsius for 30 min from the Sabin 1 and 2 viruses were isolated by repeating the process of incubation of the virus stock at 50 degrees Celsius for 30 min and multiplication of the remaining virus in a cell culture. The isolated mutants were stable genetically, and maintained the rct and d markers of the parent virus. On electron microscopical examination, the mutants were observed to retain the intact morphology after being heated at 50 degrees Celsius for 30 min, while the parent virus was converted to empty particles devoid of RNA under the same conditions. On determination of the nucleotide sequence of the P1 region, a single nucleotide sequence substitution was detected at nucleotide no. 2741, resulting in an amino acid change from valine to alanine at the 87th position of VP1. This amino acid might be associated with the heat-resistance of the mutants. Furthermore, it was found that the thermostable mutants obtained in this study, which are resistant to "high" temperature (50 degrees Celsius) for a short time (30 min), were not stable against heating at the ambient temperature (37 degrees Celsius) for a long time (5 or 7 days). This suggests that the inactivation at high temperature for a short time and that at ambient temperature for a long time involve different mechanisms.

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Section: Electron Microscopymentioning

confidence: 99%

Isolation and characterisation of poliovirus mutants resistant to heating at 50°c for 30 min

Shiomi

Urasawa

et al. 2004

Journal of Medical Virology

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“…Viruses were grown in LLC-MK 2 cells and purified native and heated virus particles were prepared as previously reported (19). The concentration of native virus was determined by the optical extinction at 260 rim, assuming an absorption coefficient of 81.6 for a 1 per cent solution: The molecular weight of poliovirus was assumed to be 8:25 × 106 (12).…”

Section: Cells and Virasesmentioning

confidence: 99%

“…In crossneutralization tests between the equine inhibitor-resistant mutants and the monospecific antibodies (22,23), it was first demonstrated that poliovirus type 1 (Mahoney strain) has :multiple antigenic sites involved in neutralization; at least five neutralization epitopes and three antigenic sites on the basis of the definition of "epitope" and "antigenic site" given by WIMMER et al (24). Since the introdnction of hybridoma technology in poliovirus studies, a number of neutralizing monoclonal antibodies have provided a valuable tool for the study of poliovirus antigenic structure (3,4,8,9,11,14,15,19). EMISI et al (9) reported the presence of six neutralization epitopes which fell into two antigenic sites on VP 1.…”

Section: Introductionmentioning

confidence: 98%

“…Previously, we prepared a neutralizing monoclonal antibody, 4 C 4, which bound to the vertices of native and heated (56°C, 30 minutes) virus particles of potiovirus (19). Later, neutralizing monoclonal antibodies (3 A 4, 4 F 2 and 5 A 10) reacting with native virus-specific surface protrusions of the virus have also been produced, in this study, the two antibodies, 4 C 4 and 4 F 2, that recognize spatially distinct antigenic sites on the poliovirus particle have been compared in respect to their precipitating and neutralizing activities.…”

Section: Introductionmentioning

confidence: 99%

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Different virus-precipitating activities of neutralizing monoclonal antibodies that recognize distinct sites of poliovirus particles

Taniguchi

Urasawa

1987

Archives of Virology

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Two neutralizing monoclonal antibodies (4 C 4 and 4 F 2) against type 1 poliovirus, Mahoney strain, recognized distinct antigenic sites of the virus particles; 4 C 4 antibody bound to vertices of native and heated (56 degrees C, 30 minutes) virus of Mahoney strain, while 4 F 2 antibody reacted with specific surface protrusions of native virus of Mahoney and Sabin strains. The difference in the location of neutralization epitopes with which the two antibodies react was confirmed in the neutralization reaction by the use of mutants resistant to 4 C 4 and 4 F 2 antibody. In immune electron microscopy, double immunodiffusion and sucrose density gradient analysis of virus-antibody complexes, the two antibodies showed a marked difference in their virus-precipitating activities. The 4 C 4 antibody recognizing vertices of the virus particle had little virus-precipitating activity. In contrast, the 4 F 2 antibody that bound to specific surface protrusions of native virus aggregated virus particle efficiently. In neutralization assays, however, the 4 C 4 antibody exhibited a slightly stronger neutralizing activity than the 4 F 2 antibody. Thus, it was suggested that the strength in precipitating activities of the two antibodies did not correlate with that in their neutralizing activities.

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“…monoclonal antibodies. In this regard, the close relationship between PRIg and monoclonal antibody was demonstrated in our recent study: reactivity of several monoclonal antibodies prepared against Mahoney strain with various PRIgresistant Mahoney strains disclosed that one of the neutralizing monoclonal antibodies, 4C4, possessed the same specificity as HN31 (18); electronmicroscopic studies revealed that the monoclonal antibody 4C4 bound only to the vertices of native and heated poliovirus particles (18) as did the HN31 antibody (19); the monoclonal antibody 4C4 failed to precipitate the virus in agar gel (20) as did both the equine serum HN31 and the HN31 antibody. These results also lead us to consider that PRIg is a kind of antibody with a chance reactivity to a definite structure resembling by chance a certain epitope of poliovirus antigen.…”

Section: Screening O F Equine and Bovine Sera By Virus Neutralizationmentioning

confidence: 99%

Comparison of Naturally Occurring Poliovirus-Reactive Immunoglobulins in Bovine and Equine Sera

Urasawa¹,

Urasawa²,

Ishizawa³

et al. 1987

JJMSB

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Monoclonal Antibodies Reactive with Different Sites of N and H Antigenic Particles of Poliovirus

Cited by 8 publications

References 13 publications

Isolation and characterisation of poliovirus mutants resistant to heating at 50°c for 30 min

Isolation and characterisation of poliovirus mutants resistant to heating at 50°c for 30 min

Different virus-precipitating activities of neutralizing monoclonal antibodies that recognize distinct sites of poliovirus particles

Comparison of Naturally Occurring Poliovirus-Reactive Immunoglobulins in Bovine and Equine Sera

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